BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 26844

Title: NMR assignments for the insertion domain of bacteriophage Sf6 coat protein   PubMed: 27798771

Deposition date: 2016-07-05 Original release date: 2018-10-03

Authors: Tripler, Therese; Teschke, Carolyn; Alexandrescu, Andrei

Citation: Tripler, Therese; Teschke, Carolyn; Alexandresu, Andrei. "NMR assignments for the insertion domain of bacteriophage Sf6 coat protein"  Biomol. NMR Assignments 11, 35-38 (2017).

Assembly members:
Sf6id, polymer, 124 residues, Formula weight is not available

Natural source:   Common Name: Sf6 Bacteriophage   Taxonomy ID: 38018   Superkingdom: Virsues   Kingdom: not available   Genus/species: Sf6 Bacteriophage

Experimental source:   Production method: recombinant technology   Host organism: Shigella flexneri

Entity Sequences (FASTA):
Sf6id: GAFGGTLTVKTQPTVTYNAV KDSYQFTVTLTGATASVTGF LKAGDQVKFTNTYWLQQQTK QALYNGATPISFTATVTADA NSDSGGDVTVTLSGVPIYDT TNPQYNSVSRQVEAGDAVSV VGTA

Data sets:
Data typeCount
13C chemical shifts448
15N chemical shifts132
1H chemical shifts754

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Sf6id1

Entities:

Entity 1, Sf6id 124 residues - Formula weight is not available

contains C-terminal 6x his-tag

1   GLYALAPHEGLYGLYTHRLEUTHRVALLYS
2   THRGLNPROTHRVALTHRTYRASNALAVAL
3   LYSASPSERTYRGLNPHETHRVALTHRLEU
4   THRGLYALATHRALASERVALTHRGLYPHE
5   LEULYSALAGLYASPGLNVALLYSPHETHR
6   ASNTHRTYRTRPLEUGLNGLNGLNTHRLYS
7   GLNALALEUTYRASNGLYALATHRPROILE
8   SERPHETHRALATHRVALTHRALAASPALA
9   ASNSERASPSERGLYGLYASPVALTHRVAL
10   THRLEUSERGLYVALPROILETYRASPTHR
11   THRASNPROGLNTYRASNSERVALSERARG
12   GLNVALGLUALAGLYASPALAVALSERVAL
13   VALGLYTHRALA

Samples:

sample_1: insertion domain, [U-100% 15N], 1.5 mM; insertion domain, [U-100% 13C; U-100% 15N], 2.1 mM; H2O 90%; D2O 10%

sample_2: insertion domain, [U-100% 13C; U-100% 15N], 2.1 mM; D2O 100%

sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC NH2 onlysample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
HNCACOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
2D DQF-COSYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

Ccpnmr_analysis, CCPN - chemical shift assignment, peak picking

Felix, Accelrys Software Inc. - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts